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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Structure-Function Insights into Anionic and Cationic Undecapeptides: A Combined Modeling and Antibacterial Study.

Thang Nguyen Quoc1, Hai Bui Thi Phuong2, Duc Nguyen Van3

  • 1Faculty of Pharmaceutical Chemistry and Technology, Hanoi University of Pharmacy, Hanoi, 10000, Vietnam.

The Journal of Membrane Biology
|May 20, 2026
PubMed
Summary

Positive charge and helical structure are key for antimicrobial peptides (AMPs) to disrupt bacterial membranes. This study shows cationic BP52 is effective, while anionic AMPs are not, guiding future drug design.

Keywords:
BP52Cn-AMP2Antimicrobial peptidesMD simulationMembrane-active peptides

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Antimicrobial peptides (AMPs) are a vital alternative to conventional antibiotics.
  • Understanding AMP structure-activity relationships is crucial for developing new therapeutics.

Purpose of the Study:

  • To compare the structural and functional properties of three synthetic undecapeptides.
  • To investigate the antibacterial activity and membrane interaction mechanisms of anionic and cationic AMPs.

Main Methods:

  • Synthesis and characterization of three undecapeptides: Cn-AMP2, Ac-CnAMP2, and BP52.
  • In vitro antibacterial assays against Gram-positive and Gram-negative bacteria.
  • Hemolysis assays to assess red blood cell toxicity.
  • Molecular dynamics simulations to analyze membrane interactions.

Main Results:

  • Cationic BP52 demonstrated potent antibacterial activity against both bacterial types.
  • Anionic Cn-AMP2 and Ac-CnAMP2 exhibited no significant antibacterial effects.
  • BP52 showed mild to moderate hemolytic activity, while anionic peptides were non-hemolytic.
  • Molecular dynamics simulations revealed BP52's superior membrane insertion, clustering, and disruption capabilities.

Conclusions:

  • Positive charge, helical conformation, and amphipathic structure are critical for AMPs' membrane-disrupting activity.
  • Findings provide insights for designing more effective and targeted AMP-based therapeutics.
  • This research highlights the potential of cationic AMPs as next-generation antibiotics.